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The study of bound-state conformations of ligands interacting with proteins is important to the understanding of protein function and the design of drugs that alter function. Traditionally, transferred nuclear Overhauser effects (trNOEs), measured from NMR spectra of ligands in rapid exchange between bound and free states, have been used in these studies, owing to the inherent heavy weighting of bound state data in the averaged ligand signals. In principle, residual dipolar couplings (RDCs)doi:10.1021/ja069145h pmid:17385862 pmcid:PMC2542485 fatcat:wxxpzlxhdvdn5kdvdee7fdktfi